Giant multilevel cation channels formed by Alzheimer disease amyloid beta-protein [A beta P-(1-40)] in bilayer membranes
about
Alzheimer's disease; taking the edge off with cannabinoids?Amyloid-beta Alzheimer targets - protein processing, lipid rafts, and amyloid-beta poresIntracellular Calcium Dysregulation: Implications for Alzheimer's DiseaseMolecular Structure, Membrane Interactions, and Toxicity of the Islet Amyloid Polypeptide in Type 2 Diabetes MellitusStructural evolution and membrane interactions of Alzheimer's amyloid-beta peptide oligomers: new knowledge from single-molecule fluorescence studiesEstablishing Natural Nootropics: Recent Molecular Enhancement Influenced by Natural NootropicAmyloid oligomer neurotoxicity, calcium dysregulation, and lipid raftsComparative modeling of hypothetical amyloid pores based on cylindrin.Models of membrane-bound Alzheimer's Abeta peptide assembliesAnti-Viral Properties of Amyloid-β Peptides.Membrane interactions of a self-assembling model peptide that mimics the self-association, structure and toxicity of Abeta(1-40).Biophysical insights into how surfaces, including lipid membranes, modulate protein aggregation related to neurodegeneration.Exploring the mechanism of beta-amyloid toxicity attenuation by multivalent sialic acid polymers through the use of mathematical models.Cholesterol is an important factor affecting the membrane insertion of beta-amyloid peptide (A beta 1-40), which may potentially inhibit the fibril formation.Clues to neuro-degeneration in Niemann-Pick type C disease from global gene expression profilingMembrane localization of beta-amyloid 1-42 in lysosomes: a possible mechanism for lysosome labilizationStructure-function relationships of pre-fibrillar protein assemblies in Alzheimer's disease and related disordersCalcium signaling and amyloid toxicity in Alzheimer disease.Simultaneous single-molecule fluorescence and conductivity studies reveal distinct classes of Abeta species on lipid bilayersAmyloid-beta-induced ion flux in artificial lipid bilayers and neuronal cells: resolving a controversyCalcium ions promote formation of amyloid β-peptide (1-40) oligomers causally implicated in neuronal toxicity of Alzheimer's disease.Activity and architecture of pyroglutamate-modified amyloid-β (AβpE3-42) poresAmyloid ion channels: a common structural link for protein-misfolding diseaseAlzheimer's disease amyloid beta-protein forms Zn(2+)-sensitive, cation-selective channels across excised membrane patches from hypothalamic neurons.Computational study of hippocampal-septal theta rhythm changes due to β-amyloid-altered ionic channelsStructural convergence among diverse, toxic beta-sheet ion channels.Beta-amyloid peptide blocks the fast-inactivating K+ current in rat hippocampal neurons.Theoretical models of the ion channel structure of amyloid beta-protein.Late-onset Alzheimer's disease, heating up and foxed by several proteins: pathomolecular effects of the aging process.Transmembrane glycine zippers: physiological and pathological roles in membrane proteins.Disordered amyloidogenic peptides may insert into the membrane and assemble into common cyclic structural motifs.Inhibition of amyloid-beta aggregation and caspase-3 activation by the Ginkgo biloba extract EGb761.Displacement currents associated with the insertion of Alzheimer disease amyloid beta-peptide into planar bilayer membranesSurface behavior and lipid interaction of Alzheimer beta-amyloid peptide 1-42: a membrane-disrupting peptideEffect of synthetic aβ peptide oligomers and fluorinated solvents on Kv1.3 channel properties and membrane conductance.Alzheimer's disease: which type of amyloid-preventing drug agents to employ?Gene identification in Alzheimer's disease.Inhibitors of catalase-amyloid interactions protect cells from beta-amyloid-induced oxidative stress and toxicity.Role of the fast kinetics of pyroglutamate-modified amyloid-β oligomers in membrane binding and membrane permeability.Multivariate analyses of amyloid-beta oligomer populations indicate a connection between pore formation and cytotoxicity
P2860
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P2860
Giant multilevel cation channels formed by Alzheimer disease amyloid beta-protein [A beta P-(1-40)] in bilayer membranes
description
1993 nî lūn-bûn
@nan
1993 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած
@hyw
1993 թվականի նոյեմբերին հրատարակված գիտական հոդված
@hy
1993年の論文
@ja
1993年学术文章
@wuu
1993年学术文章
@zh-cn
1993年学术文章
@zh-hans
1993年学术文章
@zh-my
1993年学术文章
@zh-sg
1993年學術文章
@yue
name
Giant multilevel cation channe ...... myloid beta-protein [A beta P-
@nl
Giant multilevel cation channe ...... P-(1-40)] in bilayer membranes
@ast
Giant multilevel cation channe ...... P-(1-40)] in bilayer membranes
@en
type
label
Giant multilevel cation channe ...... myloid beta-protein [A beta P-
@nl
Giant multilevel cation channe ...... P-(1-40)] in bilayer membranes
@ast
Giant multilevel cation channe ...... P-(1-40)] in bilayer membranes
@en
prefLabel
Giant multilevel cation channe ...... myloid beta-protein [A beta P-
@nl
Giant multilevel cation channe ...... P-(1-40)] in bilayer membranes
@ast
Giant multilevel cation channe ...... P-(1-40)] in bilayer membranes
@en
P2093
P2860
P356
P1476
Giant multilevel cation channe ...... P-(1-40)] in bilayer membranes
@en
P2093
P2860
P304
10573-10577
P356
10.1073/PNAS.90.22.10573
P407
P577
1993-11-01T00:00:00Z